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8J79

Bovine Xanthine Oxidoreductase Crystallized with oxypurinol

Functional Information from GO Data
ChainGOidnamespacecontents
A0002197cellular_componentxanthine dehydrogenase complex
A0004854molecular_functionxanthine dehydrogenase activity
A0004855molecular_functionxanthine oxidase activity
A0005506molecular_functioniron ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0009115biological_processxanthine catabolic process
A0016491molecular_functionoxidoreductase activity
A0030151molecular_functionmolybdenum ion binding
A0042803molecular_functionprotein homodimerization activity
A0043546molecular_functionmolybdopterin cofactor binding
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
A0071949molecular_functionFAD binding
B0002197cellular_componentxanthine dehydrogenase complex
B0004854molecular_functionxanthine dehydrogenase activity
B0004855molecular_functionxanthine oxidase activity
B0005506molecular_functioniron ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0009115biological_processxanthine catabolic process
B0016491molecular_functionoxidoreductase activity
B0030151molecular_functionmolybdenum ion binding
B0042803molecular_functionprotein homodimerization activity
B0043546molecular_functionmolybdopterin cofactor binding
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0071949molecular_functionFAD binding
Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGEGGCGAC
ChainResidueDetails
ACYS43-CYS51

site_idPS00559
Number of Residues36
DetailsMOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD
ChainResidueDetails
AGLY797-ASP832

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:15148401
ChainResidueDetails
AGLU1261
BGLU1261

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252
ChainResidueDetails
ACYS43
APHE798
AARG912
AALA1079
BCYS43
BCYS48
BCYS51
BCYS73
BCYS113
BCYS116
BCYS148
ACYS48
BCYS150
BGLN767
BPHE798
BARG912
BALA1079
ACYS51
ACYS73
ACYS113
ACYS116
ACYS148
ACYS150
AGLN767

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401
ChainResidueDetails
ALEU257
BASP360
BLEU404
BLYS422
APHE337
ASER347
AASP360
ALEU404
ALYS422
BLEU257
BPHE337
BSER347

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AGLU802
AARG880
APHE914
ATHR1010
BGLU802
BARG880
BPHE914
BTHR1010

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 139
ChainResidueDetails
AGLU802electrostatic stabiliser, hydrogen bond acceptor
AARG880electrostatic stabiliser, hydrogen bond donor
AGLU1261electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 139
ChainResidueDetails
BGLU802electrostatic stabiliser, hydrogen bond acceptor
BARG880electrostatic stabiliser, hydrogen bond donor
BGLU1261electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-17

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